2102933-95-7

Lysine-specific demethylase 1 (LSD1) belongs to the family of flavin adenine dinucleotide (FAD)-dependent amine oxidases that include monoamine oxidases (MAOs) and polyamine oxidase (PAO).¹ LSD1 specifically demethylates mono- and dimethylated histone H3 lysine 4, resulting in transcriptional repression.² It also controls the tumor suppressor activity of p53 by demethylating a specific p53 lysine residue (LYS³⁷⁰).³ GSK-LSD1 is an irreversible, mechanism-based inhibitor of LSD1 (IC₅₀ = 16 nM) that is >1,000-fold selective over the closely related FAD-utilizing enzymes LSD2, MAO-A, and MAO-B.⁴ GSK-LSD1 induces gene expression changes in various cancer cell lines, inhibiting their proliferation (EC₅₀s <5 nM).⁴ See the Structural Genomics Consortium (SGC) website for more information.

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1. Shi, Y., Lan, F., Matson, C., et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 Cell 119(7),941-953(2004).
2. Forneris, F., Binda, C., Vanoni, M.A., et al. Human histone demethylase LSD1 reads the histone code J. Biol. Chem. 280(50),41360-41365(2005).
3. Huang, J., Sengupta, R., Espejo, A.B., et al. p53 is regulated by the lysine demethylase LSD1 Nature 449,105-108(2007).
4. Epigenetics probes collection ,(2014).